Diverse Trafficking Patterns Due to Multiple Traffic Motifs in G Protein-Activated Inwardly Rectifying Potassium Channels from Brain and Heart

G protein-activated inwardly rectifying potassium channels (Kir3, GIRK) provide an important mechanism for neurotransmitter regulation of membrane excitability. GIRK channels are tetramers containing various combinations of Kir3 subunits (Kir3.1–Kir3.4). We find that different combinations of Kir3 s...

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Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 2002-02, Vol.33 (5), p.715-729
Main Authors: Ma, Dzwokai, Zerangue, Noa, Raab-Graham, Kimberly, Fried, Sharon R., Jan, Yuh Nung, Jan, Lily Yeh
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Brain - metabolism
Cells, Cultured
COS Cells
Culture Media, Serum-Free
Electrophysiology
Endocytosis - physiology
Endoplasmic Reticulum - chemistry
Endoplasmic Reticulum - metabolism
Fluorescent Dyes - metabolism
Heart
Heart - physiology
Heart rate
Hippocampus - cytology
Hippocampus - metabolism
Microscopy, Confocal
Microtubules - metabolism
Molecular Sequence Data
Neurons - cytology
Neurons - metabolism
Oocytes - physiology
Potassium
Potassium Channels, Inwardly Rectifying - chemistry
Potassium Channels, Inwardly Rectifying - metabolism
Protein Sorting Signals
Protein Subunits
Protein Transport - physiology
Proteins
Rats
Rats, Sprague-Dawley
Sequence Alignment
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Summary:G protein-activated inwardly rectifying potassium channels (Kir3, GIRK) provide an important mechanism for neurotransmitter regulation of membrane excitability. GIRK channels are tetramers containing various combinations of Kir3 subunits (Kir3.1–Kir3.4). We find that different combinations of Kir3 subunits exhibit a surprisingly complex spectrum of trafficking phenotypes. Kir3.2 and Kir3.4, but not Kir3.1, contain ER export signals that are important for plasma membrane expression of Kir3.1/Kir3.2 and Kir3.1/Kir3.4 heterotetramers, the GIRK channels found in the brain and the heart, respectively. Additional motifs in Kir3.2 and Kir3.4 control the trafficking between endosome and plasma membrane. In contrast, the Kir3.3 subunit potently inhibits plasma membrane expression by diverting the heterotetrameric channels to lysosomes. Such rich trafficking behaviors provide a mechanism for dynamic regulation of GIRK channel density in the plasma membrane.
ISSN:0896-6273
1097-4199
DOI:10.1016/S0896-6273(02)00614-1